D-K6L9 is an all-D enantiomeric peptide enriched in lysine and leucine residues arranged for amphipathic helix formation. D-configuration confers strong resistance to proteolysis while preserving membrane-interaction potential. Researchers explore its folding, aggregation, and antimicrobial-like properties in vitro. Applications include D-peptide design, stability studies, and membrane-active motif development.
CAT No: R2793
CAS No:426264-61-1
Synonyms/Alias:D-K6L9; 426264-61-1; HY-P5924A; DA-62931; CS-0896345;
D-K6L9 is a synthetic antimicrobial peptide engineered for research applications in molecular biology, microbiology, and peptide science. Structurally, it is a D-enantiomeric analog of the parent K6L9 peptide, designed to enhance proteolytic stability and broaden its functional spectrum. As a member of the host defense peptide family, D-K6L9 exhibits amphipathic properties and a net positive charge, characteristics that underpin its interaction with microbial membranes. Its resistance to enzymatic degradation makes it particularly valuable for in vitro and in vivo studies aiming to dissect peptide-membrane dynamics, antimicrobial mechanisms, and peptide engineering strategies. The unique sequence and stereochemistry of D-K6L9 provide researchers with a robust tool for investigating peptide function and developing novel peptide-based technologies.
Antimicrobial mechanism studies: D-K6L9 is widely employed in the investigation of antimicrobial mechanisms, particularly those involving membrane disruption and bacterial cell lysis. Its ability to interact with lipid bilayers and selectively target microbial membranes enables detailed exploration of peptide-induced permeability, pore formation, and membrane destabilization. Researchers utilize D-K6L9 to elucidate the structure-activity relationships governing antimicrobial efficacy, thereby advancing the understanding of innate immune peptides and informing the rational design of next-generation antimicrobial agents.
Peptide stability and proteolytic resistance assays: The D-amino acid configuration of D-K6L9 confers significant resistance to proteolytic enzymes, a property that is critical for studies focused on peptide stability and longevity in biological environments. By comparing the degradation profiles of D-K6L9 with its L-enantiomeric counterparts, scientists can assess the impact of stereochemistry on peptide half-life, metabolic fate, and resistance to enzymatic cleavage. These insights are essential for optimizing peptide therapeutics, delivery systems, and diagnostic reagents.
Biofilm inhibition research: D-K6L9 is a valuable tool in biofilm-related studies, where it serves as a model compound for evaluating anti-biofilm activity and mechanisms of action. Its capacity to disrupt established biofilms and inhibit biofilm formation is leveraged in experimental systems to investigate the molecular determinants of biofilm resilience and susceptibility. Such research is instrumental in the development of strategies to combat persistent microbial communities in medical, industrial, and environmental settings.
Peptide-membrane interaction analysis: The amphipathic nature and defined charge distribution of D-K6L9 make it an excellent candidate for detailed biophysical studies of peptide-membrane interactions. Techniques such as circular dichroism spectroscopy, fluorescence assays, and electron microscopy are employed to characterize its binding affinity, insertion depth, and conformational dynamics within model membranes. These analyses provide critical data for understanding the physicochemical principles that govern peptide selectivity and activity at the membrane interface.
Peptide engineering and structure-activity relationship (SAR) studies: D-K6L9 serves as a reference compound in peptide engineering efforts aimed at optimizing antimicrobial potency, selectivity, and stability. Through systematic sequence modifications and comparative SAR analyses, researchers use D-K6L9 as a benchmark to assess the functional consequences of specific amino acid substitutions, stereochemical alterations, and sequence motifs. The knowledge gained from such studies informs the design of novel peptide scaffolds with tailored biological properties for advanced research and biotechnological applications.
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